3GFJ
Crystal structure of the ST1710 mutant (R89A) protein
Summary for 3GFJ
| Entry DOI | 10.2210/pdb3gfj/pdb |
| Related | 2eb7 2yrs 3GFL 3GFM 3gez 3gf2 3gfi |
| Descriptor | 146aa long hypothetical transcriptional regulator, CALCIUM ION (3 entities in total) |
| Functional Keywords | transcription regulator, st1710, marr, dna-binding, transcription, transcription regulation, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi |
| Biological source | Sulfolobus tokodaii |
| Total number of polymer chains | 1 |
| Total formula weight | 16833.53 |
| Authors | Kumarevel, T.,Tanaka, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-02-27, release date: 2009-08-25, Last modification date: 2023-11-01) |
| Primary citation | Kumarevel, T.,Tanaka, T.,Umehara, T.,Yokoyama, S. ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators. Nucleic Acids Res., 37:4723-4735, 2009 Cited by PubMed Abstract: ST1710, a member of the multiple antibiotic resistance regulator (MarR) family of regulatory proteins in bacteria and archaea, plays important roles in development of antibiotic resistance, a global health problem. Here, we present the crystal structure of ST1710 from Sulfolobus tokodaii strain 7 complexed with salicylate, a well-known inhibitor of MarR proteins and the ST1710 complex with its promoter DNA, refined to 1.8 and 2.10 A resolutions, respectively. The ST1710-DNA complex shares the topology of apo-ST1710 and MarR proteins, with each subunit containing a winged helix-turn-helix (wHtH) DNA binding motif. Significantly large conformational changes occurred upon DNA binding and in each of the dimeric monomers in the asymmetric unit of the ST1710-DNA complex. Conserved wHtH loop residues interacting with the bound DNA and mutagenic analysis indicated that R89, R90 and K91 were important for DNA recognition. Significantly, the bound DNA exhibited a new binding mechanism. PubMed: 19509310DOI: 10.1093/nar/gkp496 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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